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Biological Activation of Heteropoly Complex of Molybdotungstosilicate Containing Lanthanum K10H3La(SiMo6W5O39)2⋅26H2O: Spectroscopic Approach and Microcalorimetry

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Abstract

In this paper, the biological activation of heteropoly complex of molybdotungstosilicate containing lanthanum K10H3La(SiMo6W5O39)2⋅26H2O (LaW5) was investigated by spectroscopic approach and microcalorimetry under the human physiological conditions. Fluorescence spectroscopy in combination with UV–Vis absorption spectroscopy was employed to investigate the binding of LaW5 to bovine serum albumin (BSA). In the mechanism discussion, it was proved that the fluorescence quenching of BSA by LaW5 is a result of the formation of LaW5–BSA complex. Binding parameters were determined using the Stern–Volmer equation. The results of thermodynamic parameters ∆G, ∆H, ∆S at different temperatures indicate that van der Waals interactions and hydrogen bonds play a major role for LaW5–BSA association. The distance r between donor (BSA) and acceptor (LaW5) was obtained according to fluorescence resonance energy transfer. Furthermore, the calorimetric method was used to monitor the biological activity of LaW5 in Escherichia coli.

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Acknowledgments

The authors gratefully acknowledge financial support of National Natural Science Foundation of China (grants no. 20803019, 20873096, and 20621502), the Research Foundation of Education Bureau of Hubei Province, China (grant no. Q20082205), and Hubei Normal University Foundation, China (grant no. 2007F10).

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Correspondence to Yi Liu.

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Hu, YJ., Ou-Yang, Y., Zhao, RM. et al. Biological Activation of Heteropoly Complex of Molybdotungstosilicate Containing Lanthanum K10H3La(SiMo6W5O39)2⋅26H2O: Spectroscopic Approach and Microcalorimetry. Biol Trace Elem Res 135, 314–324 (2010). https://doi.org/10.1007/s12011-009-8493-8

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